Taurine dioxygenase
| taurine dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.11.17 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
| |||||||||
In enzymology, a taurine dioxygenase (EC 1.14.11.17) is an enzyme that catalyzes the chemical reaction
- taurine + 2-oxoglutarate + O2 sulfite + aminoacetaldehyde + succinate + CO2
The 3 substrates of this enzyme are taurine, 2-oxoglutarate, and O2, whereas its 4 products are sulfite, aminoacetaldehyde, succinate, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is taurine, 2-oxoglutarate:O2 oxidoreductase (sulfite-forming). Other names in common use include 2-aminoethanesulfonate dioxygenase, and alpha-ketoglutarate-dependent taurine dioxygenase. This enzyme participates in taurine and hypotaurine metabolism. It has 3 cofactors: iron, Ascorbate, and Fe2+.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1GQW, 1GY9, 1OS7, and 1OTJ.
References
- Eichhorn E, van der Ploeg JR, Kertesz MA, Leisinger T (1997). "Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli". J. Biol. Chem. 272 (37): 23031–6. doi:10.1074/jbc.272.37.23031. PMID 9287300.